1rqf

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Revision as of 23:40, 20 November 2007

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spinqualitylabelsall models 1rqf, resolution 2.89Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structure of CK2 beta subunit crystallized in the presence of a p21WAF1 peptide

Overview

A truncated form of the regulatory subunit of the protein kinase CK2beta, (residues 1-178) has been crystallized in the presence of a fragment of, the cyclin-dependent kinase inhibitor p21WAF1 (residues 46-65) and the, structure solved at 2.9 A resolution by molecular replacement. The core of, the CK2beta dimer shows a high structural similarity with that identified, in previous structural analyses of the dimer and the holoenzyme. However, the electron density corresponding to the substrate-binding acidic loop, (residues 55-64) indicates two conformations that differ from that of the, holoenzyme structure [Niefind et al. (2001), EMBO J. 20, 5320-5331]., Difference electron density near the dimerization region in each of the, eight protomers in the asymmetric unit is attributed to between one and, eight amino-acid residues of a complexed fragment of p21WAF1. This binding, site corresponds to the solvent-accessible part of the conserved, zinc-finger motif.

About this Structure

1RQF is a Single protein structure of sequence from Xenopus laevis with ZN and UNK as ligands. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.

Reference

Structure of the regulatory subunit of CK2 in the presence of a p21WAF1 peptide demonstrates flexibility of the acidic loop., Bertrand L, Sayed MF, Pei XY, Parisini E, Dhanaraj V, Bolanos-Garcia VM, Allende JE, Blundell TL, Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1698-704. Epub, 2004 Sep 23. PMID:15388915

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